ID A0A2A3LJN0_9GAMM Unreviewed; 450 AA.
AC A0A2A3LJN0;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Xaa-Pro dipeptidase {ECO:0000256|HAMAP-Rule:MF_01279};
DE Short=X-Pro dipeptidase {ECO:0000256|HAMAP-Rule:MF_01279};
DE EC=3.4.13.9 {ECO:0000256|HAMAP-Rule:MF_01279};
DE AltName: Full=Imidodipeptidase {ECO:0000256|HAMAP-Rule:MF_01279};
DE AltName: Full=Proline dipeptidase {ECO:0000256|HAMAP-Rule:MF_01279};
DE Short=Prolidase {ECO:0000256|HAMAP-Rule:MF_01279};
GN Name=pepQ {ECO:0000256|HAMAP-Rule:MF_01279};
GN ORFNames=CMZ84_12115 {ECO:0000313|EMBL:PBJ82979.1};
OS Xanthomonadaceae bacterium NML93-0399.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae.
OX NCBI_TaxID=2032565 {ECO:0000313|EMBL:PBJ82979.1, ECO:0000313|Proteomes:UP000218035};
RN [1] {ECO:0000313|EMBL:PBJ82979.1, ECO:0000313|Proteomes:UP000218035}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NML93-0399 {ECO:0000313|EMBL:PBJ82979.1,
RC ECO:0000313|Proteomes:UP000218035};
RA Bernier A.-M., Bernard K.;
RT "Clinical and environmental strains of Xanthomonadaceae.";
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Splits dipeptides with a prolyl residue in the C-terminal
CC position. {ECO:0000256|HAMAP-Rule:MF_01279}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + Xaa-L-Pro dipeptide = an L-alpha-amino acid + L-proline;
CC Xref=Rhea:RHEA:76407, ChEBI:CHEBI:15377, ChEBI:CHEBI:59869,
CC ChEBI:CHEBI:60039, ChEBI:CHEBI:195196; EC=3.4.13.9;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01279};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01279};
CC Note=Binds 2 manganese ions per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_01279};
CC -!- SIMILARITY: Belongs to the peptidase M24B family. Bacterial-type
CC prolidase subfamily. {ECO:0000256|HAMAP-Rule:MF_01279}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PBJ82979.1}.
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DR EMBL; NTJI01000002; PBJ82979.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A3LJN0; -.
DR OrthoDB; 9806388at2; -.
DR Proteomes; UP000218035; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008235; F:metalloexopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016795; F:phosphoric triester hydrolase activity; IEA:InterPro.
DR GO; GO:0102009; F:proline dipeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 1.
DR Gene3D; 3.40.350.10; Creatinase/prolidase N-terminal domain; 1.
DR HAMAP; MF_01279; X_Pro_dipeptid; 1.
DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR048819; PepQ_N.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS.
DR InterPro; IPR022846; X_Pro_dipept.
DR PANTHER; PTHR43226; XAA-PRO AMINOPEPTIDASE 3; 1.
DR PANTHER; PTHR43226:SF4; XAA-PRO AMINOPEPTIDASE 3; 1.
DR Pfam; PF21216; PepQ_N; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
DR PROSITE; PS00491; PROLINE_PEPTIDASE; 1.
PE 3: Inferred from homology;
KW Dipeptidase {ECO:0000256|ARBA:ARBA00022997, ECO:0000256|HAMAP-
KW Rule:MF_01279};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01279};
KW Manganese {ECO:0000256|ARBA:ARBA00023211, ECO:0000256|HAMAP-Rule:MF_01279};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01279};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049, ECO:0000256|HAMAP-
KW Rule:MF_01279};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_01279}.
FT DOMAIN 8..158
FT /note="Xaa-Pro dipeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF21216"
FT DOMAIN 170..430
FT /note="Peptidase M24"
FT /evidence="ECO:0000259|Pfam:PF00557"
FT BINDING 247
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01279"
FT BINDING 258
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01279"
FT BINDING 258
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01279"
FT BINDING 339
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01279"
FT BINDING 384
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01279"
FT BINDING 423
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01279"
FT BINDING 423
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01279"
SQ SEQUENCE 450 AA; 48973 MW; 46A64F90193FAC59 CRC64;
MPAPSAASLY ADHLATLQTR AATALERAGL DHLVIPSGTV HYQVFDDRDY PYAVNPHFKA
WLPLTRTPGS WLVVTPGARP KLIYLQPRDY WHVVPDAPSG YWVEHFDIVV IRKPEDAQQH
LPRNAARCAI LGEPQSALGQ YGAYKPNNPQ AVVDHLDYHR AFKTPYELAM LRAANRHAVR
AHRAAERAFR AGASEFGIHL AYCQAAGQDA NELPYGNIVA LNEHAAVLHY TELGRLAPDP
VRSFLIDAGA SHAGYAADVT RTWAADTGSE FQSMIDAVDT AQQAMVAQVR AGTDYRQIHL
DAHLALSGVL RDFGVLRVSP EEAVATGVSA AFFPHGIGHG IGLQVHDVGG FIAAETGGAI
AKPDGHPYLR LTRTLAADMV VTIEPGVYFI DMLLEDLRSA GKGDAVDWDR IEAFKPYGGI
RIEDDVVCTD DAPENLTRDA WAQDVADTAD
//
